TSPNThrombospondin N-terminal -like domains.
|SMART accession number:||SM00210|
|Description:||Heparin-binding and cell adhesion domain of thrombospondin|
|Interpro abstract (IPR001791):|
Laminins are large heterotrimeric glycoproteins involved in basement membrane function [(PUBMED:15037599)]. The Laminin G or LNS domain (for Laminin-alpha, Neurexin and Sex hormone-binding globulin) is an around 180 amino acid long domain found in a large and diverse set of extracellular proteins [(PUBMED:1975589), (PUBMED:9480764)]. The laminin globular (G) domain can be found in one to several copies in various laminin family members, including a large number of extracellular proteins. The C terminus of the laminin alpha chain contains a tandem repeat of five laminin G domains, which are critical for heparin-binding and cell attachment activity [(PUBMED:10747011)]. Laminin alpha4 is distributed in a variety of tissues including peripheral nerves, dorsal root ganglion, skeletal muscle and capillaries; in the neuromuscular junction, it is required for synaptic specialisation [(PUBMED:15823034)]. The structure of the laminin-G domain has been predicted to resemble that of pentraxin [(PUBMED:9480764)].
Laminin G domains can vary in their function, and a variety of binding functions have been ascribed to different LamG modules. For example, the laminin alpha1 and alpha2 chains each have five C-teminal laminin G domains, where only domains LG4 and LG5 contain binding sites for heparin, sulphatides and the cell surface receptor dystroglycan [(PUBMED:10747011)]. Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion, signalling, migration, assembly and differentiation. Proteins with laminin-G domains include:
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